AMPDB_120 | Cathepsin G
PEPTIDE SUMMARY
Cathepsin G
1 General Description
AMPDB ID: AMPDB_120
Protein Names: Cathepsin G (CG) (EC 3.4.21.20) [Cleaved into: Cathepsin G; C-terminal truncated form]
Protein Family: Peptidase S1 family
Gene Name: CTSG
Source Organism: Homo sapiens (Human)
Protein Length: 255 AA
Protein Existence: Evidence at protein level
2 Protein Sequence & Composition
2.1 Sequence
MQPLLLLLAFLLPTGAEAGEIIGGRESRPHSRPYMAYLQIQSPAGQSRCGGFLVREDFVLTAAHCWGSNINVTLGAHNIQRRENTQQHITARRAIRHPQYNQRTIQNDIMLLQLSRRVRRNRNVNPVALPRAQEGLRPGTLCTVAGWGRVSMRRGTDTLREVQLRVQRDRQCLRIFGSYDPRRQICVGDRRERKAAFKGDSGGPLLCNNVAHGIVSYGKSSGVPPEVFTRVSSFLPWIRTTMRSFKLLDQMETPL
FASTA format
2.2 Composition
Counts of Amino Acids
'A': 16, 'R': 34, 'N': 11, 'D': 8, 'C': 6, 'Q': 17, 'E': 10, 'G': 22, 'H': 6, 'I': 13, 'L': 26, 'K': 4, 'M': 6, 'F': 8, 'P': 15, 'S': 15, 'T': 14, 'W': 3, 'Y': 5, 'V': 16
Frequencies of Amino Acids
'A': 6.27%, 'R': 13.33%, 'N': 4.31%, 'D': 3.14%, 'C': 2.35%, 'Q': 6.67%, 'E': 3.92%, 'G': 8.63%, 'H': 2.35%, 'I': 5.1%, 'L': 10.2%, 'K': 1.57%, 'M': 2.35%, 'F': 3.14%, 'P': 5.88%, 'S': 5.88%, 'T': 5.49%, 'W': 1.18%, 'Y': 1.96%, 'V': 6.27%
Missing Amino Acid(s)
No Amino Acid(s) are missing in this protein
Most Occurring Amino Acid(s)
R
Less Occurring Amino Acid(s)
W
Hydrophobic Amino Acid(s) Count
125
Hydrophilic Amino Acid(s) Count
130
Basic Amino Acid(s) Count
18
Acidic Amino Acid(s) Count
44
Modified Amino Acid(s) Count
0
Modified Amino Acid(s) Frequencies
0
Computed by biopython (version 1.79) & proteinAnalysis (version 1)
3 Physicochemical Properties
Sl. No. Properties Values Reference
1. Molecular Mass 28837.2 Da Computed by ProtParam module (biopython 1.79)
2. Aliphatic Index 84.118 Computed by ProtParam module (biopython 1.79)
3. Instability Index (Half Life) 60.87 Computed by ProtParam module (biopython 1.79)
4. Hydrophobicity (GRAVY) -0.433 Computed by ProtParam module (biopython 1.79)
5. Hydrophobic Moment 0.797 Computed by ProtParam module (biopython 1.79)
6. Isoelectric Point 11.693 Computed by ProtParam module (biopython 1.79)
7. Charge (at pH 7) 20.187 Computed by ProtParam module (biopython 1.79)
8. Secondary Structure Fraction 0.278, 0.247, 0.227 [Helix, Turn, Sheet] Computed by ProtParam module (biopython 1.79)
9. Aromaticity 0.063 Computed by ProtParam module (biopython 1.79)
10. Molar Extinction Coefficient (cysteine|cystine) 23950, 24325 Computed by ProtParam module (biopython 1.79)
4 Activity Details
4.1 Target Organism(s)
L.monocytogenes (Gram-positive), M.tuberculosis (Gram-positive), N.gonorrhoeae (Gram-negative), P.aeruginosa (Gram-negative), S.aureus (Gram-positive), T.denticola (Gram-negative)
4.2 Antimicrobial Activity
Antibiotic, Antimicrobial, Anti-biofilm, Anti-tuberculosis, Anti-gram-negative, Anti-gram-Positive
4.3 Enzymatic Activity
Hydrolase, Protease, Serine protease
4.4 Inhibitory Effect
Not found
4.5 Other Biological Activity
Cell membrane, Chemotaxis, Cytotoxin, Proteolytic, Non-hemolytic, Non-ribosomal
Activity data manually curated from Literature and UniProt
5 Database Cross-references
5.1 Literature Database
5.1.1 PubMed
Citation 1: Salvesen G, Farley D, Shuman J, et al. Molecular cloning of human cathepsin G: structural similarity to mast cell and cytotoxic T lymphocyte proteinases. Biochemistry. 1987;26(8):2289-93. Published 1987 Apr 21. doi:10.1021/bi00382a032
PMID: 3304423
Citation 2: Hohn PA, Popescu NC, Hanson RD, et al. Genomic organization and chromosomal localization of the human cathepsin G gene. J Biol Chem. 1989;264(23):13412-9. Published 1989 Aug 15. doi:
PMID: 2569462
Citation 3: Gerhard DS, Wagner L, Feingold EA, et al. The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004;14(10B):2121-7. Published 2004 Oct. doi:10.1101/gr.2596504
PMID: 15489334
Citation 4: Avril LE, Di Martino-Ferrer M, Pignede G, et al. Identification of the U-937 membrane-associated proteinase interacting with the V3 loop of HIV-1 gp120 as cathepsin G. FEBS Lett. 1994;345(1):81-6. Published 1994 May 23. doi:10.1016/0014-5793(94)00410-2
PMID: 8194606
Citation 5: Heck LW, Rostand KS, Hunter FA, et al. Isolation, characterization, and amino-terminal amino acid sequence analysis of human neutrophil cathepsin G from normal donors. Anal Biochem. 1986;158(1):217-27. Published 1986 Oct. doi:10.1016/0003-2697(86)90612-3
PMID: 3799965
Citation 6: Gabay JE, Scott RW, Campanelli D, et al. Antibiotic proteins of human polymorphonuclear leukocytes. Proc Natl Acad Sci U S A. 1989;86(14):5610-4. Published 1989 Jul. doi:10.1073/pnas.86.14.5610
PMID: 2501794
Citation 7: Maison CM, Villiers CL, Colomb MG, et al. Proteolysis of C3 on U937 cell plasma membranes. Purification of cathepsin G. J Immunol. 1991;147(3):921-6. Published 1991 Aug 1. doi:
PMID: 1861080
Citation 8: Gaskin G, Kendal H, Coulthart A, et al. Use of proteinase 3 purified by reverse phase HPLC to detect autoantibodies in systemic vasculitis. J Immunol Methods. 1995;180(1):25-33. Published 1995 Mar 13. doi:10.1016/0022-1759(94)00295-8
PMID: 7897245
Citation 9: Loke I, Packer NH, Thaysen-Andersen M, et al. Complementary LC-MS/MS-Based N-Glycan, N-Glycopeptide, and Intact N-Glycoprotein Profiling Reveals Unconventional Asn71-Glycosylation of Human Neutrophil Cathepsin G. Biomolecules. 2015;5(3):1832-54. Published 2015 Aug 12. doi:10.3390/biom5031832
PMID: 26274980
Citation 10: Selak MA, Chignard M, Smith JB, et al. Cathepsin G is a strong platelet agonist released by neutrophils. Biochem J. 1988;251(1):293-9. Published 1988 Apr 1. doi:10.1042/bj2510293
PMID: 3390156
Citation 11: Salvesen G, Enghild JJ, Enghild JJ. An unusual specificity in the activation of neutrophil serine proteinase zymogens. Biochemistry. 1990;29(22):5304-8. Published 1990 Jun 5. doi:10.1021/bi00474a013
PMID: 2383548
Citation 12: Bangalore N, Travis J, Onunka VC, et al. Identification of the primary antimicrobial domains in human neutrophil cathepsin G. J Biol Chem. 1990;265(23):13584-8. Published 1990 Aug 15. doi:
PMID: 2116408
Citation 13: Alford CE, Amaral E, Campbell PA, et al. Listericidal activity of human neutrophil cathepsin G. J Gen Microbiol. 1990;136(6):997-100. Published 1990 Jun. doi:10.1099/00221287-136-6-997
PMID: 2117044
Citation 14: Shafer WM, Onunka VC, Jannoun M, et al. Molecular mechanism for the antigonococcal action of lysosomal cathepsin G. Mol Microbiol. 1990;4(8):1269-77. Published 1990 Aug. doi:10.1111/j.1365-2958.1990.tb00706.x
PMID: 2126324
Citation 15: Wasiluk KR, Skubitz KM, Gray BH, et al. Comparison of granule proteins from human polymorphonuclear leukocytes which are bactericidal toward Pseudomonas aeruginosa. Infect Immun. 1991;59(11):4193-200. Published 1991 Nov. doi:10.1128/iai.59.11.4193-4200.1991
PMID: 1937776
Citation 16: Hase-Yamazaki T, Aoki Y, Aoki Y. Stimulation of human lymphocytes by cathepsin G. Cell Immunol. 1995;160(1):24-32. Published 1995 Jan. doi:10.1016/0008-8749(95)80005-4
PMID: 7842483
Citation 17: Molino M, Blanchard N, Belmonte E, et al. Proteolysis of the human platelet and endothelial cell thrombin receptor by neutrophil-derived cathepsin G. J Biol Chem. 1995;270(19):11168-75. Published 1995 May 12. doi:10.1074/jbc.270.19.11168
PMID: 7744748
Citation 18: Garwicz D, Lindmark A, Gullberg U, et al. Human cathepsin G lacking functional glycosylation site is proteolytically processed and targeted for storage in granules after transfection to the rat basophilic/mast cell line RBL or the murine myeloid cell line 32D. J Biol Chem. 1995;270(47):28413-8. Published 1995 Nov 24. doi:10.1074/jbc.270.47.28413
PMID: 7499346
Citation 19: Plescia J, Altieri DC, Altieri DC. Activation of Mac-1 (CD11b/CD18)-bound factor X by released cathepsin G defines an alternative pathway of leucocyte initiation of coagulation. Biochem J. 1996;319 ( Pt 3)(Pt 3):873-9. Published 1996 Nov 1. doi:10.1042/bj3190873
PMID: 8920993
Citation 20: Yamazaki T, Aoki Y, Aoki Y. Cathepsin G binds to human lymphocytes. J Leukoc Biol. 1997;61(1):73-9. Published 1997 Jan. doi:10.1002/jlb.61.1.73
PMID: 9000539
Citation 21: Yamazaki T, Aoki Y, Aoki Y. Cathepsin G enhances human natural killer cytotoxicity. Immunology. 1998;93(1):115-21. Published 1998 Jan. doi:10.1046/j.1365-2567.1998.00397.x
PMID: 9536127
Citation 22: Sambrano GR, Huang W, Faruqi T, et al. Cathepsin G activates protease-activated receptor-4 in human platelets. J Biol Chem. 2000;275(10):6819-23. Published 2000 Mar 10. doi:10.1074/jbc.275.10.6819
PMID: 10702240
Citation 23: Biggs JR, Yang J, Gullberg U, et al. The human brm protein is cleaved during apoptosis: the role of cathepsin G. Proc Natl Acad Sci U S A. 2001;98(7):3814-9. Published 2001 Mar 27. doi:10.1073/pnas.071057398
PMID: 11259672
Citation 24: Rivera-Marrero CA, Stewart J, Shafer WM, et al. The down-regulation of cathepsin G in THP-1 monocytes after infection with Mycobacterium tuberculosis is associated with increased intracellular survival of bacilli. Infect Immun. 2004;72(10):5712-21. Published 2004 Oct. doi:10.1128/IAI.72.10.5712-5721.2004
PMID: 15385470
Citation 25: Sun R, Iribarren P, Zhang N, et al. Identification of neutrophil granule protein cathepsin G as a novel chemotactic agonist for the G protein-coupled formyl peptide receptor. J Immunol. 2004;173(1):428-36. Published 2004 Jul 1. doi:10.4049/jimmunol.173.1.428
PMID: 15210802
Citation 26: Burster T, Beck A, Tolosa E, et al. Cathepsin G, and not the asparagine-specific endoprotease, controls the processing of myelin basic protein in lysosomes from human B lymphocytes. J Immunol. 2004;172(9):5495-503. Published 2004 May 1. doi:10.4049/jimmunol.172.9.5495
PMID: 15100291
Citation 27: Lim JK, Lu W, Hartley O, et al. N-terminal proteolytic processing by cathepsin G converts RANTES/CCL5 and related analogs into a truncated 4-68 variant. J Leukoc Biol. 2006;80(6):1395-404. Published 2006 Dec. doi:10.1189/jlb.0406290
PMID: 16963625
Citation 28: Mambole A, Baruch D, Nusbaum P, et al. The cleavage of neutrophil leukosialin (CD43) by cathepsin G releases its extracellular domain and triggers its intramembrane proteolysis by presenilin/gamma-secretase. J Biol Chem. 2008;283(35):23627-35. Published 2008 Aug 29. doi:10.1074/jbc.M710286200
PMID: 18586676
Citation 29: Gale AJ, Rozenshteyn D, Rozenshteyn D. Cathepsin G, a leukocyte protease, activates coagulation factor VIII. Thromb Haemost. 2008;99(1):44-51. Published 2008 Jan. doi:10.1160/TH07-08-0495
PMID: 18217133
Citation 30: Burkard TR, Planyavsky M, Kaupe I, et al. Initial characterization of the human central proteome. BMC Syst Biol. 2011;5:17. Published 2011 Jan 26. doi:10.1186/1752-0509-5-17
PMID: 21269460
Citation 31: Danelishvili L, Everman JL, McNamara MJ, et al. Inhibition of the Plasma-Membrane-Associated Serine Protease Cathepsin G by Mycobacterium tuberculosis Rv3364c Suppresses Caspase-1 and Pyroptosis in Macrophages. Front Microbiol. 2011;2:281. Published 2011. doi:10.3389/fmicb.2011.00281
PMID: 22275911
Citation 32: Woloszynek JC, Hu Y, Pham CT, et al. Cathepsin G-regulated release of formyl peptide receptor agonists modulate neutrophil effector functions. J Biol Chem. 2012;287(41):34101-9. Published 2012 Oct 5. doi:10.1074/jbc.M112.394452
PMID: 22879591
Citation 33: Lefrançais E, Roga S, Gautier V, et al. IL-33 is processed into mature bioactive forms by neutrophil elastase and cathepsin G. Proc Natl Acad Sci U S A. 2012;109(5):1673-8. Published 2012 Jan 31. doi:10.1073/pnas.1115884109
PMID: 22307629
Citation 34: Vaca Jacome AS, Rabilloud T, Schaeffer-Reiss C, et al. N-terminome analysis of the human mitochondrial proteome. Proteomics. 2015;15(14):2519-24. Published 2015 Jul. doi:10.1002/pmic.201400617
PMID: 25944712
Citation 35: Jun HK, Jung YJ, Ji S, et al. Caspase-4 activation by a bacterial surface protein is mediated by cathepsin G in human gingival fibroblasts. Cell Death Differ. 2018;25(2):380-391. Published 2018 Feb. doi:10.1038/cdd.2017.167
PMID: 29077095
Citation 36: Thorpe M, Fu Z, Chahal G, et al. Extended cleavage specificity of human neutrophil cathepsin G: A low activity protease with dual chymase and tryptase-type specificities. PLoS One. 2018;13(4):e0195077. Published 2018. doi:10.1371/journal.pone.0195077
PMID: 29652924
Citation 37: Guo J, Tu J, Hu Y, et al. Cathepsin G cleaves and activates IL-36γ and promotes the inflammation of psoriasis. Drug Des Devel Ther. 2019;13:581-588. Published 2019. doi:10.2147/DDDT.S194765
PMID: 30804664
Citation 38: Huang S, Thomsson KA, Jin C, et al. Cathepsin g Degrades Both Glycosylated and Unglycosylated Regions of Lubricin, a Synovial Mucin. Sci Rep. 2020;10(1):4215. Published 2020 Mar 6. doi:10.1038/s41598-020-61161-5
PMID: 32144329
Citation 39: Huang S, Thomsson KA, Jin C, et al. Author Correction: Cathepsin g Degrades Both Glycosylated and Unglycosylated Regions of Lubricin, a Synovial Mucin. Sci Rep. 2021;11(1):4238. Published 2021 Feb 15. doi:10.1038/s41598-020-77619-5
PMID: 33589665
Citation 40: Kavanaugh JS, Leidal KG, Nauseef WM, et al. Cathepsin G Degrades Staphylococcus aureus Biofilms. J Infect Dis. 2021;223(11):1865-1869. Published 2021 Jun 4. doi:10.1093/infdis/jiaa612
PMID: 32995850
Citation 41: Hof P, Mayr I, Huber R, et al. The 1.8 A crystal structure of human cathepsin G in complex with Suc-Val-Pro-PheP-(OPh)2: a Janus-faced proteinase with two opposite specificities. EMBO J. 1996;15(20):5481-91. Published 1996 Oct 15. doi:
PMID: 8896442
Citation 42: Greco MN, Hawkins MJ, Powell ET, et al. Nonpeptide inhibitors of cathepsin G: optimization of a novel beta-ketophosphonic acid lead by structure-based drug design. J Am Chem Soc. 2002;124(15):3810-1. Published 2002 Apr 17. doi:10.1021/ja017506h
PMID: 11942800
Citation 43: de Garavilla L, Greco MN, Sukumar N, et al. A novel, potent dual inhibitor of the leukocyte proteases cathepsin G and chymase: molecular mechanisms and anti-inflammatory activity in vivo. J Biol Chem. 2005;280(18):18001-7. Published 2005 May 6. doi:10.1074/jbc.M501302200
PMID: 15741158
Citation 44: Herdendorf TJ, Stapels DAC, Rooijakkers SHM, et al. Local structural plasticity of the Staphylococcus aureus evasion protein EapH1 enables engagement with multiple neutrophil serine proteases. J Biol Chem. 2020;295(22):7753-7762. Published 2020 May 29. doi:10.1074/jbc.RA120.013601
PMID: 32303641
Citation 45: Lüdecke B, Poller W, Olek K, et al. Sequence variant of the human cathepsin G gene. Hum Genet. 1993;91(1):83-4. Published 1993 Mar. doi:10.1007/BF00230230
PMID: 8454293
5.2 Protein Sequence Databases
UniProt: P08311
5.3 3D Structure Databases
AlphaFoldDB: P08311
5.4 Nucleotide Sequence Databases
Sl. no. Accession(s) Access Link(s)
1. M16117 GenBank || EMBL
2. J04990 GenBank || EMBL
3. CR456807 GenBank || EMBL
4. CR541704 GenBank || EMBL
5. CH471078 GenBank || EMBL
6. BC014460 GenBank || EMBL
RefSeq: NP_001902.1
5.5 Protein-Protein Interaction Databases
IntAct: P08311
MINT: P08311
DIP: Not found
BioGRID: 107891
5.6 Ligand Databases
BindingDB: P08311
DrugBank: DB04016, DB02360
ChEMBL: CHEMBL4071
5.7 Family & Domain Databases
PANTHER: Not found
5.8 Genome Annotation Databases
KEGG: hsa:1511
5.9 Phylogenomic Databases
5.10 Enzyme & Pathway Databases
BRENDA: 3.4.21.20
BioCyc: Not found
5.11 Protein-RNA Interaction Databases
RNAct: P08311




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